An atypical alcohol dehydrogenase was found in two human livers. The anomalous enzyme, which has been purified, differs from the normal regarding (a) pH rate profile, (b) substrate specificity, and (c) sensitivity to metal binding agents. Thiourea inhibits the variant enzyme, but activates normal human liver alcohol dehydrogenase. A simple screening test is described to differentiate between atypical and normal alcohol dehydrogenase in liver homogenate. Total alcohol dehydrogenase activity was considerably higher in livers containing the atypical enzyme.

No abstract

No abstract

Ethanol utilization by the isolated perfused rat liver was studied under various experimental conditions. 1. A linear decrease of the ethanol concentration in the perfusing medium was observed, indicating that ethanol utilization was independent of the ethanol concentration. 2. Inhibition of alcohol dehydrogenase by pyrazol was paralleled by a decrease in ethanol utilization. 3. The uptake of fructose and its conversion to glucose were inhibited by ethanol. Ethanol utilization was diminished in the presence of fructose. 4. Increased ratios of lactate to pyruvate and a-glycerophosphate to dihydroxyacetone phosphate were found during ethanol oxidation. These changes are presumably due to the formation of NADH, although they were not prevented by an inhibition of alcohol dehydrogenase with pyrazol.

No abstract